[1]	NUCLEOTIDE SEQUENCE [MRNA]. Hostetler C.E., Robison M.R., Kincaid R.L., Ott T.L.; "Sus scrofa selenium-containing enzyme cytosolic glutathione peroxidase 1 (cGPX1) from the day 13 embryo."; Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Protects the hemoglobin in erythrocytes from oxidative breakdown (By similarity).
CATALYTIC ACTIVITY: 2 glutathione + H₂O₂ = glutathione disulfide + 2 H₂O.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the glutathione peroxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF532927; AAM94630.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_999366.1; -.

UniGene

Ssc.6352

3D structure databases

SMR

Q8MJ14; 17-200.

ModBase

Q8MJ14.

Protein family/group databases

PeroxiBase

3722; SscGPx01.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004602;	Molecular function: glutathione peroxidase activity (inferred from electronic annotation from InterPro).
GO:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006979;	Biological process: response to oxidative stress (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000889; Glut_peroxidase.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 1.

PANTHER

PTHR11592; Glut_peroxidase; 1.

Pfam

PF00255; GSHPx; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000303; Glutathion_perox; 1.

PRINTS

PR01011; GLUTPROXDASE.

PROSITE

PS00460; GLUTATHIONE_PEROXID_1; 1.
PS00763; GLUTATHIONE_PEROXID_2; 1.
PS51355; GLUTATHIONE_PEROXID_3; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8MJ14.

Genome annotation databases

GeneID

397403; -.

KEGG

ssc:397403; -.

Phylogenomic databases

HOVERGEN

Q8MJ14; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Oxidoreductase; Peroxidase; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 206`	`206`	`Glutathione peroxidase 1.`	`PRO_0000066614`
`ACT_SITE`	`52 52`		`By similarity.`
`NON_STD`	`52 52`		`Selenocysteine.`
`MOD_RES`	`151 151`		`N6-acetyllysine (By similarity).`

Sequence information

Length: 206 AA [This is the length of the unprocessed precursor]

Molecular weight: 22591 Da [This is the MW of the unprocessed precursor]

CRC64: 4431BECD35A797A0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MCAAQRSAAA LAAVAPRSVY AFSARPLAGG EPISLGSLRG KVLLIENVAS LUGTTVRDYT 

        70         80         90        100        110        120 
QMNELQRRLG PRGLVVLGFP CNQFGHQENA KNGEILNCLK YVRPGGGFEP NFMLFEKCEV 

       130        140        150        160        170        180 
NGANAHPLFA FLREALPTPS DDATALMTDP KFITWSPVCR NDIAWNFEKF LVGPDGVPLR 

       190        200 
RYSRRFLTID IEPDIEALLS QEPSSA

Q8MJ14 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools